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dc.contributor.author
Tosso, Rodrigo David
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Zarycz, Maria Natalia Cristina
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Schiel, María Ayelén
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Goicoechea Moro, Luisa
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Baldoni, Hector Armando
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Angelina, Emilio Luis
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Enriz, Ricardo Daniel
dc.date.available
2023-09-19T11:00:07Z
dc.date.issued
2022-05
dc.identifier.citation
Tosso, Rodrigo David; Zarycz, Maria Natalia Cristina; Schiel, María Ayelén; Goicoechea Moro, Luisa; Baldoni, Hector Armando; et al.; Evaluating the conformational space of the active site of D2 dopamine receptor. Scope and limitations of the standard docking methods; John Wiley & Sons; Journal of Computational Chemistry; 43; 19; 5-2022; 1298-1312
dc.identifier.issn
0192-8651
dc.identifier.uri
http://hdl.handle.net/11336/211936
dc.description.abstract
We report here for the first time the potential energy surfaces (PES) of phenyletilamine (PEA) and meta-tyramine (m-OH-PEA) at the D2 dopamine receptor (D2DR) binding site. PESs not only allow us to observe all the critical points of the surface (minimums, maximums, and transition states), but also to note the ease or difficulty that each local minima have for their conformational inter-conversions and therefore know the conformational flexibility that these ligands have in their active sites. Taking advantage of possessing this valuable information, we analyze how accurate a standard docking study is in these cases. Our results indicate that although we have to be careful in how to carry out this type of study and to consider performing some extra-simulations, docking calculations can be satisfactory. In order to analyze in detail the different molecular interactions that are stabilizing the different ligand-receptor (L-R) complexes, we carried out quantum theory of atoms in molecules (QTAIM) computations and NMR shielding calculations. Although some of these techniques are a bit tedious and require more computational time, our results demonstrate the importance of performing computational simulations using different types of combined techniques (docking/MD/hybrid QM-MM/QTAIM and NMR shielding calculations) in order to obtain more accurate results. Our results allow us to understand in details the molecular interactions stabilizing and destabilizing the different L-R complexes reported here. Thus, the different activities observed for dopamine (DA), m-OH-PEA, and PEA can be clearly explained at molecular level.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
John Wiley & Sons
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
D2 DOPAMINE RECEPTOR
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PHENYLETILAMINE
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POTENTIAL ENERGY SURFACES
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QTAIM ANALYSIS
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RESONANCE ASSISTED HYDROGEN BOND
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Otras Ciencias Químicas
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Ciencias Químicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Evaluating the conformational space of the active site of D2 dopamine receptor. Scope and limitations of the standard docking methods
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2023-06-29T17:52:24Z
dc.journal.volume
43
dc.journal.number
19
dc.journal.pagination
1298-1312
dc.journal.pais
Estados Unidos
dc.description.fil
Fil: Tosso, Rodrigo David. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina
dc.description.fil
Fil: Zarycz, Maria Natalia Cristina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina
dc.description.fil
Fil: Schiel, María Ayelén. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina
dc.description.fil
Fil: Goicoechea Moro, Luisa. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina
dc.description.fil
Fil: Baldoni, Hector Armando. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina
dc.description.fil
Fil: Angelina, Emilio Luis. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Modelado e Innovación Tecnológica. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Modelado e Innovación Tecnológica; Argentina
dc.description.fil
Fil: Enriz, Ricardo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
dc.journal.title
Journal of Computational Chemistry
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/10.1002/jcc.26938
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1002/jcc.26938
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